1ku8

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1ku8, resolution 1.75Å

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Crystal structure of Jacalin

Overview

Evidence is presented that the specificity of jacalin, the seed lectin, from jack fruit (Artocarpus integrifolia), is not directed exclusively, against the T-antigen disaccharide Galbeta1,3GalNAc, lactose and, galactose, but also against mannose and oligomannosides. Biochemical, analyses based on surface-plasmon-resonance measurements, combined with, the X-ray-crystallographic determination of the structure of a, jacalin-alpha-methyl-mannose complex at 2 A resolution, demonstrated, clearly that jacalin is fully capable of binding mannose. Besides mannose, jacalin also interacts readily with glucose, N-acetylneuraminic acid and, N-acetylmuramic acid. Structural analyses demonstrated that the relatively, large size of the carbohydrate-binding site enables jacalin to accommodate, monosaccharides with different hydroxyl conformations and provided, unambiguous evidence that the beta-prism structure of jacalin is a, sufficiently flexible structural scaffold to confer different, carbohydrate-binding specificities to a single lectin.

About this Structure

1KU8 is a Protein complex structure of sequences from Artocarpus integer. Full crystallographic information is available from OCA.

Reference

Structural basis for the unusual carbohydrate-binding specificity of jacalin towards galactose and mannose., Bourne Y, Astoul CH, Zamboni V, Peumans WJ, Menu-Bouaouiche L, Van Damme EJ, Barre A, Rouge P, Biochem J. 2002 May 15;364(Pt 1):173-80. PMID:11988090

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